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Persistent URL http://purl.org/net/epubs/work/44103
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Record Id 44103
Title Anharmonic Behavior in the Multisubunit Protein Apoferritin as Revealed by Quasi-Elastic Neuton Scattering
Abstract Quasi-elastic neutron scattering (QENS) has been used to study the deviation from Debye-law harmonic behavior in lyophilized and hydrated apoferritin, a naturally occurring, multisubunit protein. Whereas analysis of the measured mean squared displacement (msd) parameter reveals a hydration-dependent inflection above 240 K, characteristic of diffusive motion, a hydration-independent inflection is observed at 100 K. The mechanism responsible for this low-temperature anharmonic response is further investigated, via analysis of the elastic incoherent neutron scattering intensity, by applying models developed to describe side-group motion in glassy polymers. Our results suggest that the deviation from harmonic behavior is due to the onset of methyl group rotations which exhibit a broad distribution of activated processes Our results are likened to those reported for other proteins
Organisation ISIS , ISIS-OSIRIS , STFC
Keywords Physics , apoferritin , Chemistry , quasi-elastic neutron scattering , proteins , methyl group rotation , Biology
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Language English (EN)
Type Details URI(s) Local file(s) Year
Journal Article J Phys Chem B 112, no. 35 (2008): 10873-10878. doi:10.1021/jp801779x 2008
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